Porcine cyclic peptide lysine is a convenient compound that can be used to develop various porcine cyclic peptide derivatives that can be used to study cell structure and other biological applications. It reacts easily with amine reactive dyes, biotin and other label molecules such as NHS esters, isothiocyanates and sulfonyl chloride, among others. Ghost pen cyclic peptide is a bicyclic heptapeptidine toxin that specifically binds to the interface between F-actin subunits, locking adjacent subunits together. Ghost cyclin binds to the actin filament much more tightly than to the actin monomer, resulting in a decrease in the rate constant at which the actin subunits dissociate from the filament end, thereby essentially stabilizing the actin filament by preventing the filament from depolymerizing. The properties of ghost ring peptides are a useful tool for studying the distribution of F-actin in cells by labeling ghost ring peptides with fluorescent analogs and using them to stain actin filaments for optical microscopy. Fluorescent derivatives of ghost cyclic peptides have proven to be very useful in locating actin filaments in living or immobilizing cells, as well as in visualizing individual actin filaments in vitro. Fluorophosphorin derivatives have been used as important tools to study actin networks at high resolution.

Study the distribution of F-actin in cells.